Protein profile

PA5410

protein GbcA

Genome: NC_002516.2

Gene: gbcA PA5410 Structure source: AlphaFold UniProt Q9HTF4

Export view

Amino acids 429

Annotations 6

Features 29

PDB binders 9

Druggability 0.707

Overview

Basic information about this protein and its source genome.

Accession: PA5410
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: gbcA PA5410
Status: annotated
Amino acids: 429
Structure source: AlphaFold

1.14.13.251

GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0005506 Binding to an iron (Fe) ion. GO:0004497 Catalysis of the incorporation of one atom of molecular oxygen (O2) into the substrate and the reduction of the other atom of O2 to water. GO:0031457 The chemical reactions and pathways resulting in the breakdown of glycine betaine, N-trimethylglycine. GO:0044237 OBSOLETE. The chemical reactions and pathways by which individual cells transform chemical substances.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.707

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MDVTSTLSLGDPLEPARKATADMLRSRDHSFSLPQPFYCDQRLFEIDMQEIFHKEWLIAGMTCEIPAKGNFLTLQIGKNPVLVIRGAEGQVHAFHNVCRHRGSRLCVSEKGKVAKLVCPYHQWTYELDGRLLFAGTEMGADFDMKEYGLKPIQVKTAGGYIFISLAENPPAIDDFLATLEHYMEPYDMENAKVAVQTTIREAANWKLVIENNRECYHCNGSHPELLKTLLEWDDVTDPRASQAFKDQVAACTSAWDAEKIPYAHASFGLRNRIVRMPLLDGTVSMTMDGKQGSKKLMGRIKNPDLGSMRILHLPHSWNHCMGDHLIVFTVWPISAQETLVTTKWLVHKDAVEGVDYDVARLREVWDATNDQDRRLAEENQRGINSDAYQPGPYSKTYEFGVINFLDWYSERMLNNLGEESAHVRKVAGS

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1.14.13.251

Gene Ontology (GO)

GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0005506 Binding to an iron (Fe) ion.
GO:0004497 Catalysis of the incorporation of one atom of molecular oxygen (O2) into the substrate and the reduction of the other atom of O2 to water.
GO:0031457 The chemical reactions and pathways resulting in the breakdown of glycine betaine, N-trimethylglycine.
GO:0044237 OBSOLETE. The chemical reactions and pathways by which individual cells transform chemical substances.

Sequence Features

Domain/signature hits from InterPro and related databases.

29 records

Show feature table

Start	End	DB	Term	Name
53	172	FunFam	G3DSA:2.102.10.10:FF:000020	Aromatic ring-hydroxylating dioxygenase subunit alpha
24	167	SUPERFAMILY	SSF50022	ISP domain
24	167	InterPro	IPR036922	Rieske [2Fe-2S] iron-sulphur domain superfamily
56	131	Pfam	PF00355	Rieske [2Fe-2S] domain
56	131	InterPro	IPR017941	Rieske [2Fe-2S] iron-sulphur domain
40	65	PRINTS	PR00090	Ring hydroxylating dioxygenase alpha-subunit signature
40	65	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
189	211	PRINTS	PR00090	Ring hydroxylating dioxygenase alpha-subunit signature
189	211	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
91	111	PRINTS	PR00090	Ring hydroxylating dioxygenase alpha-subunit signature
91	111	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
152	178	PRINTS	PR00090	Ring hydroxylating dioxygenase alpha-subunit signature
152	178	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
70	85	PRINTS	PR00090	Ring hydroxylating dioxygenase alpha-subunit signature
70	85	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
112	132	PRINTS	PR00090	Ring hydroxylating dioxygenase alpha-subunit signature
112	132	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
56	163	ProSiteProfiles	PS51296	Rieske [2Fe-2S] iron-sulfur domain profile.
56	163	InterPro	IPR017941	Rieske [2Fe-2S] iron-sulphur domain
56	171	CDD	cd03469	Rieske_RO_Alpha_N
168	416	SUPERFAMILY	SSF55961	Bet v1-like
185	412	CDD	cd08884	RHO_alpha_C_GbcA-like
31	408	Gene3D	G3DSA:3.90.380.10	-
17	419	PANTHER	PTHR43756	CHOLINE MONOOXYGENASE, CHLOROPLASTIC
17	419	InterPro	IPR001663	Aromatic-ring-hydroxylating dioxygenase, alpha subunit
189	412	Pfam	PF00848	Ring hydroxylating alpha subunit (catalytic domain)
189	412	InterPro	IPR015879	Aromatic-ring-hydroxylating dioxygenase, alpha subunit, C-terminal domain
53	172	Gene3D	G3DSA:2.102.10.10	-
53	172	InterPro	IPR036922	Rieske [2Fe-2S] iron-sulphur domain superfamily

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

Legend High Medium Low

Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA5410	AlphaFold	—	—	full sequence	—	Viewing

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
12				0.707
2				0.412

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

59 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
152	6Y9C	D0C9N6	162.2 Da LogP -0.47 TPSA 57.5	✓ Ro5	✓ Clean	`C[N+](C)(C)C[C@@H](CC(=O)O)O`
1IT	2YFJ	P37333	168.2 Da LogP 3.59 TPSA 13.1	✓ Ro5	✓ Clean	`c1ccc2c(c1)c3ccccc3o2`
3BY	4QUP	Q92ZP9	129.2 Da LogP 0.17 TPSA 40.5	✓ Ro5	✓ Clean	`CN1CCC[C@H]1C(=O)O`
AZI	4QUQ	Q92ZP9	42.0 Da LogP 0.87 TPSA 58.7	✓ Ro5	Alert	`[N-]=[N+]=[N-]`
BNL	2XRX	P37333	154.2 Da LogP 3.35 TPSA 0.0	✓ Ro5	✓ Clean	`c1ccc(cc1)c2ccccc2`
DC4	2YFL	P37333	202.6 Da LogP 4.24 TPSA 13.1	✓ Ro5	✓ Clean	`c1ccc2c(c1)c3cc(ccc3o2)Cl`
DC5	2XSH	P37333	223.1 Da LogP 4.66 TPSA 0.0	✓ Ro5	✓ Clean	`c1ccc(cc1)c2c(cccc2Cl)Cl`
FES	6Y9C	D0C9N6	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
OXY	4QUR	Q92ZP9	32.0 Da LogP 0.07 TPSA 34.1	✓ Ro5	✓ Clean	`O=O`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC2010357	1.000	223.1 Da LogP 4.66 TPSA 0.0	✓ Ro5	✓ Clean	`Clc1cccc(Cl)c1-c1ccccc1`
ZINC4798194	1.000	202.6 Da LogP 4.24 TPSA 13.1	✓ Ro5	✓ Clean	`Clc1ccc2oc3ccccc3c2c1`
ZINC4428485	0.783	237.1 Da LogP 4.89 TPSA 13.1	✓ Ro5	✓ Clean	`Clc1ccc2oc3ccc(Cl)cc3c2c1`
ZINC13776258	0.769	202.6 Da LogP 4.24 TPSA 13.1	✓ Ro5	✓ Clean	`Clc1ccc2c(c1)oc1ccccc12`
ZINC4713695	0.724	230.6 Da LogP 3.60 TPSA 30.2	✓ Ro5	✓ Clean	`O=c1c2ccccc2oc2ccc(Cl)cc12`
ZINC4077508	0.684	212.3 Da LogP 4.32 TPSA 13.1	✓ Ro5	✓ Clean	`S=c1c2ccccc2oc2ccccc12`
ZINC1638387	0.667	230.7 Da LogP 3.60 TPSA 30.2	✓ Ro5	✓ Clean	`O=c1oc2ccc(Cl)cc2c2ccccc12`
ZINC4262222	0.636	218.3 Da LogP 4.74 TPSA 13.1	✓ Ro5	✓ Clean	`c1ccc2cc3c(cc2c1)oc1ccccc13`
ZINC144320882	0.615	216.7 Da LogP 3.82 TPSA 17.1	✓ Ro5	✓ Clean	`O=Cc1cccc(Cl)c1-c1ccccc1`
ZINC169609522	0.609	294.1 Da LogP 4.19 TPSA 13.1	✓ Ro5	✓ Clean	`Ic1ccc2c(c1)oc1ccccc12`
ZINC3875601	0.609	247.1 Da LogP 4.35 TPSA 13.1	✓ Ro5	✓ Clean	`Brc1ccc2oc3ccccc3c2c1`
ZINC4416808	0.609	294.1 Da LogP 4.19 TPSA 13.1	✓ Ro5	✓ Clean	`Ic1ccc2oc3ccccc3c2c1`
ZINC5046083	0.609	247.1 Da LogP 4.35 TPSA 13.1	✓ Ro5	✓ Clean	`Brc1ccc2c(c1)oc1ccccc12`
ZINC4183097	0.607	265.1 Da LogP 4.25 TPSA 30.2	✓ Ro5	✓ Clean	`O=c1c2cc(Cl)ccc2oc2ccc(Cl)cc12`
ZINC1603007	0.600	245.3 Da LogP 4.60 TPSA 26.0	✓ Ro5	✓ Clean	`Nc1ccc(-c2ccc(-c3ccccc3)cc2)cc1`
ZINC881607888	0.600	214.3 Da LogP 1.04 TPSA 23.6	✓ Ro5	✓ Clean	`CN1CCC[C@H]1C(=O)N1CCC(F)CC1`
ZINC967435	0.600	233.1 Da LogP 4.12 TPSA 0.0	✓ Ro5	✓ Clean	`Brc1ccc(-c2ccccc2)cc1`
ZINC980089	0.600	280.1 Da LogP 3.96 TPSA 0.0	✓ Ro5	✓ Clean	`Ic1ccc(-c2ccccc2)cc1`
ZINC4805116	0.591	211.2 Da LogP 2.88 TPSA 45.7	✓ Ro5	✓ Clean	`ON=c1c2ccccc2oc2ccccc12`
ZINC5379482	0.591	210.2 Da LogP 2.36 TPSA 51.5	✓ Ro5	✓ Clean	`NN=c1c2ccccc2oc2ccccc12`
ZINC83407191	0.583	311.7 Da LogP 3.02 TPSA 52.2	✓ Ro5	✓ Clean	`Cn1c(=O)c2c3ccccc3oc3ccc(Cl)cc3c=2c1=O`
ZINC170877414	0.581	279.4 Da LogP 0.55 TPSA 43.9	✓ Ro5	✓ Clean	`CN1CCC[C@H]1C(=O)N1CCN(C(=O)C2CCC2)CC1`
ZINC195163670	0.581	293.4 Da LogP 0.94 TPSA 43.9	✓ Ro5	✓ Clean	`CN1CCC[C@@H]1C(=O)N1CCN(C(=O)C2CCCC2)CC1`
ZINC195163684	0.581	293.4 Da LogP 0.94 TPSA 43.9	✓ Ro5	✓ Clean	`CN1CCC[C@H]1C(=O)N1CCN(C(=O)C2CCCC2)CC1`
ZINC334287038	0.581	214.3 Da LogP 0.66 TPSA 23.6	✓ Ro5	✓ Clean	`CN1CCC[C@H]1C(=O)N1CCSCC1`
ZINC38236631	0.565	294.1 Da LogP 4.19 TPSA 13.1	✓ Ro5	✓ Clean	`Ic1cccc2oc3ccccc3c12`
ZINC4798839	0.565	247.1 Da LogP 4.35 TPSA 13.1	✓ Ro5	✓ Clean	`Brc1cccc2oc3ccccc3c12`
ZINC4991219	0.565	218.3 Da LogP 4.74 TPSA 13.1	✓ Ro5	✓ Clean	`c1ccc2c(c1)ccc1oc3ccccc3c12`
ZINC5935067	0.565	202.6 Da LogP 4.24 TPSA 13.1	✓ Ro5	✓ Clean	`Clc1cccc2oc3ccccc3c12`
ZINC16123618	0.563	231.3 Da LogP 4.42 TPSA 12.9	✓ Ro5	✓ Clean	`c1ccc(-c2ccc(-c3ccncc3)cc2)cc1`
ZINC4344119	0.563	211.3 Da LogP 3.09 TPSA 39.2	✓ Ro5	✓ Clean	`NCCc1ccc2oc3ccccc3c2c1`
ZINC4798226	0.563	217.7 Da LogP 3.82 TPSA 39.2	✓ Ro5	✓ Clean	`Nc1cc2oc3ccccc3c2cc1Cl`
ZINC1857794216	0.559	316.1 Da LogP 4.74 TPSA 51.8	✓ Ro5	✓ Clean	`Clc1nc(Cl)nc(-c2ccc3oc4ccccc4c3c2)n1`
ZINC44137926	0.552	270.3 Da LogP 0.47 TPSA 81.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1CCCN1CCC[C@H]1C(=O)O`
ZINC44137928	0.552	312.4 Da LogP 1.64 TPSA 81.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1CCCCCCN1CCC[C@H]1C(=O)O`
ZINC44137930	0.552	326.4 Da LogP 2.03 TPSA 81.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1CCCCCCCN1CCC[C@H]1C(=O)O`
ZINC44137933	0.552	298.4 Da LogP 1.25 TPSA 81.1	✓ Ro5	✓ Clean	`O=C(O)[C@@H]1CCCN1CCCCCN1CCC[C@H]1C(=O)O`
ZINC38042624	0.548	212.3 Da LogP 0.63 TPSA 43.8	✓ Ro5	✓ Clean	`CN1CCC(N2CCC[C@@H]2C(=O)O)CC1`
ZINC38042625	0.548	212.3 Da LogP 0.63 TPSA 43.8	✓ Ro5	✓ Clean	`CN1CCC(N2CCC[C@H]2C(=O)O)CC1`
ZINC5935064	0.548	237.1 Da LogP 4.89 TPSA 13.1	✓ Ro5	✓ Clean	`Clc1cc(Cl)c2c(c1)oc1ccccc12`
ZINC40449038	0.545	246.6 Da LogP 3.94 TPSA 50.4	✓ Ro5	✓ Clean	`O=C(O)c1ccc2oc3ccc(Cl)cc3c2c1`
ZINC489388090	0.545	434.6 Da LogP -0.15 TPSA 53.6	✓ Ro5	✓ Clean	`CN1CCC[C@@H]1C(=O)N1CCN(CCCN2CCN(C(=O)[C@H]3CCC…`
ZINC489388093	0.545	434.6 Da LogP -0.15 TPSA 53.6	✓ Ro5	✓ Clean	`CN1CCC[C@H]1C(=O)N1CCN(CCCN2CCN(C(=O)[C@H]3CCCN…`
ZINC489388096	0.545	434.6 Da LogP -0.15 TPSA 53.6	✓ Ro5	✓ Clean	`CN1CCC[C@H]1C(=O)N1CCN(CCCN2CCN(C(=O)[C@@H]3CCC…`
ZINC685940189	0.545	251.3 Da LogP -0.06 TPSA 43.9	✓ Ro5	✓ Clean	`C=CC(=O)N1CCN(C(=O)[C@H]2CCCN2C)CC1`
ZINC685940190	0.545	251.3 Da LogP -0.06 TPSA 43.9	✓ Ro5	✓ Clean	`C=CC(=O)N1CCN(C(=O)[C@@H]2CCCN2C)CC1`
ZINC95496273	0.545	275.9 Da LogP 3.96 TPSA 13.1	✓ Ro5	✓ Clean	`Brc1oc2ccccc2c1Br`
ZINC5935098	0.542	202.6 Da LogP 4.24 TPSA 13.1	✓ Ro5	✓ Clean	`Clc1cccc2c1oc1ccccc12`
ZINC6583910	0.542	247.1 Da LogP 4.35 TPSA 13.1	✓ Ro5	✓ Clean	`Brc1cccc2c1oc1ccccc12`
ZINC6583915	0.542	294.1 Da LogP 4.19 TPSA 13.1	✓ Ro5	✓ Clean	`Ic1cccc2c1oc1ccccc12`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.